Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.5: HAD, Beta-PGM, Phosphatase Like

  ⌊ C1.5.6: HAD, Beta-PGM, Phosphatase Like

     ⌊ Family phosphonoacetaldehyde hydrolase

  ⌊ FunctionalDomain phosphonoacetaldehyde hydrolase (ID 22247)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus anthracis Taxon ID: 1392 675838971 AIM10643.1 (Genbank) URP
Bacillus anthracis Taxon ID: 1392 675833562 AIM05235.1 (Genbank) URP
Bacillus anthracis str. SVA11 Taxon ID: 1392837 589080917 AHK37432.1 (Genbank) URP
Show All

Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A0E0VX83 A0A0E0VX83_BACAN (TrEMBL)
n/a C2NET5 C2NET5_BACCE (TrEMBL)

Sequence

Length of Enzyme (full-length): 267 | Length of Functional Domain: 267

1       10        20        30        40        50        60

MDCMKIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVGITAEEARKPMGLLKIDHVRAL
TEMPRIANEWNRIFGQLPTETDIQEMYEEFEEILFAILPRYASPIHGVKEVIASLRERGI
KIGSTTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNH
MIKIGDTVSDMKEGRNAGMWTVGVILGSSELGLSEEEVENMDPAELREKIEVVRNRFVEN
GAHFTIETMQELESVMERIEKQELIIS
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 2/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
12 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
126 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 2/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
12 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:12081483
160 Arg (R) side chain None -- ICS PubMed:10956028 PubMed:12081483
Family CAR This EFD conserves 8/8 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
12 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of schiff-base intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		IDA PubMed:10956028
16 Thr (T) side chain positions D29 steric role -- spectator ICS PubMed:10956028
49 Met (M) side chain involved in catalysis of schiff-base formation covalent catalysis -- reactant ICS PubMed:14670958
53 Lys (K) side chain forms schiff-base linkage to substrate covalent catalysis -- reactant IDA PubMed:9649311
56 His (H) side chain involved in catalysis of schiff-base formation covalent catalysis -- reactant ICS PubMed:14670958
126 Thr (T) side chain interacts with substrate substrate binding -- binding ICS PubMed:10956028
160 Arg (R) side chain forms salt bridge with D29 and interacts with substrate activation -- spectator ICS PubMed:10956028
186 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:10956028

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2IOF Crystal Structure Of Phosphonoacetaldehyde Hydrolase With Sodium Borohydride-Reduced Substrate Intermediate Phosphonoacetaldehyde Hydrolase • Phosphonoacetaldehyde Hydrolase 37 2.5 N~6~-Ethyl-L-Lysine
(2 more ⇓) 		CSA • PDB • PDBSum
1FEZ The Crystal Structure Of Bacillus Cereus Phosphonoacetaldehyde Hydrolase Complexed With Tungstate, A Product Analog Phosphonoacetaldehyde Hydrolase 31 3.0 Tungstate(Vi)Ion • Magnesium Ion CSA • PDB • PDBSum
1RQN Phosphonoacetaldehyde Hydrolase Complexed With Magnesium Phosphonoacetaldehyde Hydrolase 33 2.8 Magnesium Ion CSA • PDB • PDBSum
1RQL Crystal Structure Of Phosponoacetaldehyde Hydrolase Complexed With Magnesium And The Inhibitor Vinyl Sulfonate Phosphonoacetaldehyde Hydrolase 33 2.4 Magnesium Ion • Vinylsulphonic Acid CSA • PDB • PDBSum
2IOH Crystal Structure Of Phosphonoacetaldehyde Hydrolase With A K53R Mutation Phosphonoacetaldehyde Hydrolase 33 2.9 Yes Phosphate Ion • Magnesium Ion CSA • PDB • PDBSum
1SWW Crystal Structure Of The Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed With Magnesium And Substrate Phosphonoacetaldehyde Phosphonoacetaldehyde Hydrolase 33 2.3 Magnesium Ion • Phosphonoacetaldehyde CSA • PDB • PDBSum
1SWV Crystal Structure Of The D12A Mutant Of Phosphonoacetaldehyde Hydrolase Complexed With Magnesium Phosphonoacetaldehyde Hydrolase 33 2.3 Yes Magnesium Ion CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 10:09 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.